Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.7.48 (transcriptase)
 9,479 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Eleven temperature-sensitive (ts) mutants of influenza A (fowl plague, Rostock) virus were analysed for in vitro RNA transcriptase activity in reactions primed by ApG or globin mRNA at 31 degrees C or at 40.5 degrees C, the restrictive temperature for ts mutant growth. Only those ts mutants studied which were defective in RNA segment 1, coding for the virion P2 protein, were defective in RNA transcriptase activity when compared to wild-type virus. Mutants having a defect in the P2 protein had no significant RNA transcriptase activity in reactions at 40.5 degrees C primed by globin mRNA. However, one mutant showed RNA transcriptase activity similar to wild-type virus at 40.5 degrees C when ApG (0.3 mM) was used as primer. The results suggest that influenza (fowl plague, Rostock) P2 protein is directly involved in the mRNA priming reaction, as well as in the RNA transcription reaction in vitro.
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PMID:Evidence for the involvement of influenza A (fowl plague Rostock) virus protein P2 in ApG and mRNA primed in vitro RNA synthesis. 689 49

Uncovering the secretome of Yersinia pestis is a necessary measure to better understand the virulence of this plague-causing bacterium. Using bioinformatics methods, the components of all the secretion systems known to date in the Y. pestis KIM genome were mapped, including several systems identified by this study. It was found that this organism possesses Sec, twin-arginine translocation, signal recognition particle, Omp85/YaeT, type I, type II, type III, type VI, chaperone/usher, autotransporter, and two-partner secretion (TPS) systems, but lacks a type IV secretion system. The TPS systems caught the authors' attention, for they are used by several bacterial pathogens for the secretion of large virulence determinants. Reverse transcriptase-PCR analysis confirmed the gene expression of three TPS systems in Y. pestis KIM; bioinformatics studies indicated that the exoproteins of these TPS systems are putative hemolysins and adhesins. Results thus suggest that these are functional systems, capable of secreting virulence proteins that might contribute to plague infection. This is the first report on the complete secretome of pathogenic Y. pestis KIM.
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PMID:Genome-wide in silico mapping of the secretome in pathogenic Yersinia pestis KIM. 1807 74

Yersinia pestis is a pathogenic agent that causes the bubonic and pneumonic plague. The development of an efficient and low-cost oral vaccine against these diseases is highly desirable. In this study, the immunogenic fusion protein F1-V from Y. pestis was introduced into lettuce via Agrobacterium-mediated transformation, and putative transgenic lines were developed. The presence of the transgene in these putative transgenic lines was determined using polymerase chain reaction (PCR), and transgene integration and transgene copy number were confirmed following Southern blot analysis. The presence of specific F1-V transcripts was confirmed by reverse-transcriptase (RT)-PCR. Using monoclonal antibodies, ELISA and western blot analysis revealed that the expected antigenic F1-V protein was successfully expressed in transgenic lines. Mice immunized subcutaneously with lettuce expressing the F1-V antigen developed systemic humoral responses as 'proof of concept' of using lettuce as a production platform for the F1-V immunogen that could be used as a candidate plant-based vaccine against plague.
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PMID:Expression of an immunogenic F1-V fusion protein in lettuce as a plant-based vaccine against plague. 2046 3

Expression of the protective F1 and V antigens of Yersinia pestis, as a fusion protein, in carrot was pursued in an effort to develop an alternative vaccine production system against the serious plague disease. Transgenic carrot plants carrying the F1-V encoding gene were developed via Agrobacterium-mediated transformation. Presence, integration, and expression of the F1-V encoding gene were confirmed by polymerase chain reaction (PCR), DNA gel blot analysis, and reverse-transcriptase (RT)-PCR analyses, respectively. An ELISA assay confirmed the antigenicity of the plant-derived F1-V fusion protein. Immunogenicity was evaluated subcutaneously in mice using a soluble protein extract of freeze-dried transgenic carrot. Significant antibody levels were detected following immunization. These results demonstrated that the F1-V protein could be expressed in carrot tap roots, and that the carrot F1-V recombinant protein retained its antigenicity and immunogenicity.
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PMID:Transgenic carrot tap roots expressing an immunogenic F1-V fusion protein from Yersinia pestis are immunogenic in mice. 2065 21

Bovine viral diarrhea virus (BVDV) infection is still a plague that causes important livestock pandemics. Despite the availability of vaccines against BVDV, and the implementation of massive eradication or control programs, this virus still constitutes a serious agronomic burden. Therefore, the alternative approach to combat Pestivirus infections, based on the development of antiviral agents that specifically inhibit the replication of these viruses, is of preeminent actuality and importance. Capitalizing from a long-standing experience in antiviral drug design and development, in this work we present and characterize a series of small molecules based on the 9-aminoacridine scaffold that exhibit potent anti-BVDV activity coupled with low cytotoxicity. The relevant viral protein target - the RNA-dependent RNA polymerase - the binding mode, and the mechanism of action of these new antivirals have been determined by a combination of in vitro (i.e., enzymatic inhibition, isothermal titration calorimetry and site-directed mutagenesis assays) and computational experiments. The overall results obtained confirm that these acridine-based derivatives are promising compounds in the treatment of BVDV infections and, based on the reported structure-activity relationship, can be selected as a starting point for the design of a new generation of improved, safe and selective anti-BVDV agents.
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PMID:9-Aminoacridine-based agents impair the bovine viral diarrhea virus (BVDV) replication targeting the RNA-dependent RNA polymerase (RdRp). 2932 85


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